LYSC_PSEAE
ID LYSC_PSEAE Reviewed; 462 AA.
AC Q9HWK6; P82468; Q5I6A6; Q8VPA4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Lysyl endopeptidase;
DE EC=3.4.21.50;
DE AltName: Full=Protease IV;
DE AltName: Full=PvdS-regulated endoprotease;
DE Flags: Precursor;
GN Name=prpL; OrderedLocusNames=PA4175;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC CLEAVAGE, EXPRESSION IN E.COLI, AND MUTAGENESIS OF HIS-283;
RP HIS-327; ASP-333; SER-408; SER-409 AND SER-411.
RC STRAIN=PA103-29;
RX PubMed=12419815; DOI=10.1074/jbc.m208973200;
RA Traidej M., Marquart M.E., Caballero A.R., Thibodeaux B.A.,
RA O'Callaghan R.J.;
RT "Identification of the active site residues of Pseudomonas aeruginosa
RT protease IV. Importance of enzyme activity in autoprocessing and
RT activation.";
RL J. Biol. Chem. 278:2549-2553(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PA4481;
RA Parveen N., Parker D.S., Fan L., Leong J.M., Goguen J.D.;
RT "PrpL protease of Pseudomonas aeruginosa: an important virulence
RT determinant in corneal infections.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP PROTEIN SEQUENCE OF 212-226.
RA Lahnstein J.;
RL Submitted (APR-2000) to UniProtKB.
CC -!- FUNCTION: Lysine-specific endoprotease (PubMed:12419815). Involved in
CC corneal virulence. {ECO:0000305|PubMed:12419815}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.;
CC EC=3.4.21.50;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12419815}.
CC Note=Experiments performed in E.coli.
CC -!- PTM: Experiments performed in E.coli. Processing of pro-endopeptidase
CC to mature endopeptidase is probably autocatalytic, as mutations in the
CC probable active site residues prevent processing, and purified inactive
CC pro-endopeptidase disappears in the presence of active endopeptidase.
CC {ECO:0000305|PubMed:12419815}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; AY062882; AAL47683.1; -; Genomic_DNA.
DR EMBL; AY850373; AAW33983.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07562.1; -; Genomic_DNA.
DR PIR; B83123; B83123.
DR RefSeq; NP_252864.1; NC_002516.2.
DR RefSeq; WP_003112986.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWK6; -.
DR SMR; Q9HWK6; -.
DR STRING; 208964.PA4175; -.
DR MEROPS; S01.281; -.
DR PaxDb; Q9HWK6; -.
DR PRIDE; Q9HWK6; -.
DR EnsemblBacteria; AAG07562; AAG07562; PA4175.
DR GeneID; 880208; -.
DR KEGG; pae:PA4175; -.
DR PATRIC; fig|208964.12.peg.4374; -.
DR PseudoCAP; PA4175; -.
DR HOGENOM; CLU_047007_0_0_6; -.
DR OMA; ANHCIST; -.
DR BioCyc; PAER208964:G1FZ6-4248-MON; -.
DR PHI-base; PHI:3284; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:PseudoCAP.
DR GO; GO:0006554; P:lysine catabolic process; IDA:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
DR GO; GO:0006508; P:proteolysis; IDA:PseudoCAP.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Virulence; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..211
FT /evidence="ECO:0000269|Ref.4"
FT /id="PRO_0000228678"
FT CHAIN 212..462
FT /note="Lysyl endopeptidase"
FT /id="PRO_0000228679"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12419815"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12419815"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12419815"
FT DISULFID 224..435
FT /evidence="ECO:0000250"
FT DISULFID 230..305
FT /evidence="ECO:0000250"
FT DISULFID 262..284
FT /evidence="ECO:0000250"
FT MUTAGEN 283
FT /note="H->A: Loss of activity; no processing of pre-pro-
FT protein."
FT /evidence="ECO:0000269|PubMed:12419815"
FT MUTAGEN 327
FT /note="H->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:12419815"
FT MUTAGEN 333
FT /note="D->A: Loss of activity; no processing of pre-pro-
FT protein."
FT /evidence="ECO:0000269|PubMed:12419815"
FT MUTAGEN 408
FT /note="S->A: Loss of activity; no processing of pre-pro-
FT protein."
FT /evidence="ECO:0000269|PubMed:12419815"
FT MUTAGEN 409
FT /note="S->A: Loss of activity; no processing of pre-pro-
FT protein."
FT /evidence="ECO:0000269|PubMed:12419815"
FT MUTAGEN 411
FT /note="S->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:12419815"
FT CONFLICT 23
FT /note="L -> S (in Ref. 1; AAL47683)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="I -> T (in Ref. 1; AAL47683)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="T -> A (in Ref. 1; AAL47683)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="H -> R (in Ref. 1; AAL47683 and 2; AAW33983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 48213 MW; 8988A6AE53E9C816 CRC64;
MHKRTYLNAC LVLALAAGAS QALAAPGASE MAGDVAVLQA SPASTGHARF ANPNAAISAA
GIHFAAPPAR RVARAAPLAP KPGTPLQVGV GLKTATPEID LTTLEWIDTP DGRHTARFPI
SAAGAASLRA AIRLETHSGS LPDDVLLHFA GAGKEIFEAS GKDLSVNRPY WSPVIEGDTL
TVELVLPANL QPGDLRLSVP QVSYFADSLY KAGYRDGFGA SGSCEVDAVC ATQSGTRAYD
NATAAVAKMV FTSSADGGSY ICTGTLLNNG NSPKRQLFWS AAHCIEDQAT AATLQTIWFY
NTTQCYGDAS TINQSVTVLT GGANILHRDA KRDTLLLELK RTPPAGVFYQ GWSATPIANG
SLGHDIHHPR GDAKKYSQGN VSAVGVTYDG HTALTRVDWP SAVVEGGSSG SGLLTVAGDG
SYQLRGGLYG GPSYCGAPTS QRNDYFSDFS GVYSQISRYF AP
